Results 41 to 50 of about 1,426,666 (312)
The Chlamydia trachomatis Type III Secretion Chaperone Slc1 Engages Multiple Early Effectors, Including TepP, a Tyrosine-phosphorylated Protein Required for the Recruitment of CrkI-II to Nascent Inclusions and Innate Immune Signaling [PDF]
, 2014 Chlamydia trachomatis, the causative agent of trachoma and sexually transmitted infections, employs a type III secretion (T3S) system to deliver effector proteins into host epithelial cells to establish a replicative vacuole.
Bastidas, Robert J. +6 more
core +6 more sources
An improved method for surface immobilisation of RNA: application to small Non-Coding RNA - mRNA pairing [PDF]
, 2013 Characterisation of RNA and its intermolecular interactions is increasing in importance as the inventory of known RNA functions continues to expand. RNA-RNA interactions are central to post-transcriptional gene regulation mechanisms in bacteria, and the ...
Butt, Louise +9 more
core +7 more sources
Proteins That Chaperone RNA Regulation [PDF]
Microbiology Spectrum, 2018 ABSTRACT RNA-binding proteins chaperone the biological functions of noncoding RNA by reducing RNA misfolding, improving matchmaking between regulatory RNA and targets, and exerting quality control over RNP biogenesis. Recent studies of Escherichia coli CspA, HIV NCp, and E. coli Hfq
Sarah A, Woodson +2 more
openaire +2 more sources
Viruses, 2020 The 3′-terminal stem-loop (3′SL) of the RNA genome of the flavivirus West Nile (WNV) harbors, in its stem, one of the sequence elements that are required for genome cyclization.
Alexandra Meyer +7 more
doaj +1 more source
bioRxiv, 2020 RNA binding proteins play myriad roles in controlling and regulating RNAs and RNA-mediated functions, often through simultaneous binding to other cellular factors. In bacteria, the RNA chaperone Hfq modulates post-transcriptional gene regulation. Absence
Seongjin Park +7 more
semanticscholar +1 more source
Protein solubility and folding enhancement by interaction with RNA. [PDF]
PLoS ONE, 2008 While basic mechanisms of several major molecular chaperones are well understood, this machinery has been known to be involved in folding of only limited number of proteins inside the cells. Here, we report a chaperone type of protein folding facilitated
Seong Il Choi +12 more
doaj +1 more source
Nature Communications, 2022 In this work, the authors determine the crystal structure of a ProQ/FinO RNA chaperone bound to its RNA target. This provides insight into how this family of bacterial proteins recognize transcriptional terminator structures.
Hyeong Jin Kim +16 more
doaj +1 more source
Study of E. coli Hfq's RNA annealing acceleration and duplex destabilization activities using substrates with different GC-contents [PDF]
, 2012 Folding of RNA molecules into their functional three-dimensional structures is often supported by RNA chaperones, some of which can catalyse the two elementary reactions helix disruption and helix formation.
Beich-Frandsen, Mads +6 more
core +1 more source
The yeast histone chaperone hif1p functions with RNA in nucleosome assembly. [PDF]
PLoS ONE, 2014 Hif1p is an H3/H4-specific histone chaperone that associates with the nuclear form of the Hat1p/Hat2p complex (NuB4 complex) in the yeast Saccharomyces cerevisiae. While not capable of depositing histones onto DNA on its own, Hif1p can act in conjunction
Amy R Knapp, Huanyu Wang, Mark R Parthun
doaj +1 more source
Biochemistry Research International, 2011 Proteins with RNA chaperone activity are ubiquitous proteins that play important roles in cellular mechanisms. They prevent RNA from misfolding by loosening misfolded structures without ATP consumption.
Katharina Semrad
doaj +1 more source